+

WO1996035800A1 - Production enzymatique d'acide gluconique ou de ses sels - Google Patents

Production enzymatique d'acide gluconique ou de ses sels Download PDF

Info

Publication number
WO1996035800A1
WO1996035800A1 PCT/EP1996/002128 EP9602128W WO9635800A1 WO 1996035800 A1 WO1996035800 A1 WO 1996035800A1 EP 9602128 W EP9602128 W EP 9602128W WO 9635800 A1 WO9635800 A1 WO 9635800A1
Authority
WO
WIPO (PCT)
Prior art keywords
glucose
catalase
gluconic acid
conversion
process according
Prior art date
Application number
PCT/EP1996/002128
Other languages
English (en)
Inventor
Albert Joseph Vroemen
Marc Beverini
Original Assignee
Gist-Brocades B.V.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Gist-Brocades B.V. filed Critical Gist-Brocades B.V.
Priority to JP53379896A priority Critical patent/JP3910213B2/ja
Priority to CA002194859A priority patent/CA2194859C/fr
Priority to AU59983/96A priority patent/AU5998396A/en
Priority to US08/765,663 priority patent/US5897995A/en
Publication of WO1996035800A1 publication Critical patent/WO1996035800A1/fr

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0065—Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
    • C12P7/58—Aldonic, ketoaldonic or saccharic acids

Definitions

  • the present invention relates to the enzymatic production of gluconic acid. More specifically, the invention provides a method for the conversion of glucose into gluconic acid using the enzymes glucose oxidase and catalase.
  • Gluconic acid is a mild acid with many applications which comprise: its technical use as a complexing agent in industrial cleaning of metal surfaces; its use in the textile industry, in detergents and in concrete; as a food additive in beverages and also in bread and feed; and in pharmaceutical preparations as a chelating agent for ions like Fe.
  • the gluconic acid used in food applications and especially in pharmaceutical preparations must be very pure.
  • gluconic acid Up until now the production of gluconic acid at industrial scale has been carried out using a fermentation process.
  • Selected microorganisms such as e.g. Aspergillus or Gluconobacter species are grown in a fermenter which is at least equipped with air supply, pH control and temperature control. Optimal conditions are chosen for good growth of the microorganism and optimal development of the enzyme complex capable of converting glucose into gluconic acid/gluconate.
  • a glucose solution is added to the fermentation broth and aeration is continued.
  • the glucose is converted by the enzymatic complex into gluconic acid.
  • the pH is controlled by the addition of alkali, in which case the majority of gluconic acid will be present as a gluconate salt.
  • glucose is transformed into gluconic acid by an enzymatic complex consisting of glucose oxidase (Gox) and catalase.
  • Glucose oxidase catalyses the reaction:
  • the enzymes glucose oxidase and catalase are rather well characterized.
  • the glucose oxidase of A. niger is a glycoprotein with a molecular weight of about 1 50 kDa and contains prosthetic groups of FAD; the enzyme is active between pH 4 and 7 with an optimal activity at pH 5,5; the enzyme is optimally active at temperatures between 20° and 40 °C; the isoelectric point is about 4,2; the K m for glucose is 0, 1 1 M at 27°C and the K m for oxygen is 0,48 mM.
  • the catalase of A is a glycoprotein with a molecular weight of about 1 50 kDa and contains prosthetic groups of FAD; the enzyme is active between pH 4 and 7 with an optimal activity at pH 5,5; the enzyme is optimally active at temperatures between 20° and 40 °C; the isoelectric point is about 4,2; the K m for glucose is 0, 1 1 M at 27°C and the K m for oxygen is 0,48 mM.
  • niger has a molecular weight of 250 kDa; the enzyme is active between pH 2 and 7; the optimal temperature is 25 °C; the isoelectric point is about 5,4; the K m for hydrogen peroxide is about 1 , 1 M or about 37 g/l. The latter means that the affinity of the enzyme catalase for its substrate is very poor.
  • FR-A-1 590 031 describes a fermentation process for the conversion of glucose in to gluconic acid comprising the stepwise addition of glucose to the fermentation broth. Even though FR-A-1 590 031 suggests that isolated enzymes could also be applied in this process, however, it is not disclosed that this can be done using high glucose concentrations while achieving a conversion rate of more than 50 %.
  • Liu et al. ( 1 980, Proc. Natl. Sci. Counc. Repub. China 4: 338-344) use an immobilized enzyme system comprising glucose oxidase and catalase from the fungus Pullularia pullulans to convert glucose solutions of no more than
  • FR-A-2 1 77 931 discloses an enzyme-system in which catalase and glucose oxidase are immobilized in close proximity of each other in order to protect glucose oxidase from rapid inactivation by hydrogen peroxide.
  • FR-A-2 1 77 931 teaches to immobilize the enzymes in a catalase/glucose oxidase- activity ratio of at least 1 , preferably up to 200. This enzyme system is, however, only used to convert glucose solutions of no more than 5.5% glucose (w/v).
  • Hartmeier and D ⁇ ppner ( 1 983, Biotechnol. Lett. 5: 743-748; see also: D ⁇ ppner and Hartmeier, 1984, Starch 36: 283-287) use the permeabilized mycelium of a glucose oxidase and catalase producing A. niger strain which is coimmobilized with additional catalase to convert glucose into gluconic acid.
  • catalase and glucose oxidase are present in activity ratios of up to 7600 Baker Units of catalase over 2000 Sarett Units of glucose oxidase (in International catalase Units this corresponds to about a ratio of about 3950).
  • all conversions are carried out with glucose solutions of no more concentrated than 10% (w/v).
  • RO-92739 describes a process for preparing gluconic acid from glucose in a cyclic process using soluble catalase and glucose oxidase.
  • the glucose concentration used in all examples is 10% (w/v).
  • Catalase/glucose oxidase ratios of up to 200 are used to reach conversion rates of up to 98%.
  • FR-A-2 029 645 is concerned with an enzymatic process for the production of gluconic acid in which electrodialysis is used to separate glucose oxidase and the gluconic acid produced and in which hydrogen peroxide is used as oxygen donor. Subsequently fresh glucose is added to restart the reaction. This process is repeated several times. However, a dextrose equivalent of only 100 is used and the yield of gluconic acid is less than 50 %.
  • EP-A-0 01 7 708 discloses an enzymatic process in which catalase and glucose oxidase are immobilized in a ratio of at least 1 :6 in Baker Units of catalase activity and Sarett Units of glucose oxidase activity.
  • the immobilized enzymes are used to convert glucose solutions of 10% and 20% extremely low temperatures: 2°C and 8°C, respectively. Such low temperatures are, however, not economically feasible at large industrial scale because it would require immense cooling capacity in view of the exothermic nature of the reaction.
  • the present invention provides a process for the enzymatic conversion of glucose into gluconic acid, in which a glucose solution having a concentration of at least 10% (w/v) is converted into gluconic acid at good yield, viz. 50% or more, in the presence of glucose oxidase and catalase using an excess of activity units of catalase relative to oxidase and whereby the conversion takes place at a temperature of more than 10°C.
  • the present invention for the first time discloses an enzymatic process for the conversion of glucose into gluconic acid, in which a glucose solution having a concentration of at least 10% (w/v) is converted into gluconic acid in a yield of at least 50% in the presence of glucose oxidase and catalase using an excess of activity units of catalase relative to oxidase and whereby the conversion takes place at a temperature of more than 10°C.
  • the temperature at which the conversion is performed will be higher than 10°C, preferably higher than 1 5°C and more preferably 1 7°C of higher, still more preferable 20°C or higher and most preferably 25 °C or higher.
  • the upper temperature limit of the conversion will depend on the thermostability of the enzymes involved, in case the enzymes are obtainable from the fungus Aspergillus niger the temperature of the conversion should preferably be less than 40°C.
  • the glucose concentrations are herein defined as percentage weight per volume (w/v), i.e. a glucose concentration of 10 % means 100 g glucose/liter, unless indicated otherwise.
  • a glucose concentration of 10 % means 100 g glucose/liter, unless indicated otherwise.
  • gluconic acid and gluconate are used interchangeably.
  • Complete conversion is herein understood to mean that the residual glucose is less than 1 % of the original value or the conversion is more than 99 %.
  • the enzymes to be used for the conversion of glucose into gluconic acid can be all obtained from a single strain or, alternatively, can be separately obtained from different strains, and subsequently mixed to obtain the desired mixture of the enzymes involved.
  • the production strains used for the production of the enzyme preparations of the invention can be wild type strains or, alternatively, strains modified by classical mutagenesis and/or by the use recombinant DNA technology.
  • the modifications may comprise modification of the regulation of the production rate and/or production levels of the enzymes, a reduction of the level of unwanted side-activities in the enzyme preparations obtained and/or may include modification of the properties of the enzymes themselves through the use of chemical modification and/or protein engineering. Particularly advantageous are modifications which result in improved stability and/or oxidation-resistance of the enzymes to be used in the process of the invention.
  • the enzyme preparation of the invention comprises catalase and glucose oxidase and is able to convert glucose in a yield of at least 50% in an aqueous medium containing at least 25% (w/v) glucose.
  • the enzymes catalase and glucose oxidase are present in an activity ratio in excess of 200 IU/SU, respectively, wherein IU is defined as the International catalase Unit and SU is defined as the Sarett glucose oxidase Unit (see Experimental). More preferably, the activity ratio of the enzyme preparation of the invention is higher than 400 IU/SU. Even more preferable is an activity ratio in excess of 700 IU/SU.
  • the enzyme preparations of the invention are preferably applied as soluble enzymes but may also be applied as immobilized enzymes.
  • immobilized enzymes is more expensive and complicates oxygen supply.
  • Many different methods for the immobilization of glucose oxidase and/or catalase are known in the art as most work on the enzymatic conversion of glucose into gluconic acid has been performed using immobilized enzyme preparations.
  • the saccharification of polysaccharides such as starch can be combined with the conversion into a single process step or both steps can at least be performed in one and the same reactor.
  • the enzymatic complex consisting of glucose oxidase and catalase may be supplemented with enzymes capable of the conversion of non-glucose compounds into glucose.
  • examples of such enzymes are e.g. carbohydrases, such as amylases, glucoamylases, pullanases or transglucosidases, and (acid) phosphatases.
  • carbohydrases such as amylases, glucoamylases, pullanases or transglucosidases, and (acid) phosphatases.
  • at least 50% by weight of the glucose is converted into gluconic acid.
  • the reactor is preferably equipped with at least air supply, a stirring device, pH control, temperature control. More preferably, the reactor is also endowed with measurement of the dissolved oxygen concentration, the amount of air given, and the amount of oxygen in the outlet air. In this case, the oxygen consumption (which is proportional to the amount of gluconic acid produced) can be measured "on line".
  • air is used as source of oxygen in the reaction of the present invention.
  • enriched air, oxygen and/or even hydrogen peroxide are used as (additional) source of oxygen.
  • One advantage of the process of the invention is that it can be performed in the type of fermenters which are used for the fermentative production of gluconic acid, allowing a switch from the fermentative to the enzymatic process without substantial investments.
  • the preferred conditions under which the process of the invention is performed are those which are optimal for the enzymes used.
  • the preferred conditions are as follows:
  • the pH is preferably in the range between pH 4.0 and pH 7.0, more preferably between pH 5.0 and pH 6.5, most preferably the pH is set between pH 5.5 and 6.0.
  • the ratio of the activities of the enzymes catalase and glucose oxidase used in the process of the invention is higher than 2.0 IU/SU.
  • the activity ratio is higher than 55, more preferably an activity ratio in excess of 140 IU/SU is used, still more preferably the activity ratio exceeds 200 IU/SU and in the most preferred embodiment, the activity ratio is 417 IU/SU or higher.
  • a buffer can be added to the reaction mixture.
  • a phosphate buffer is used, a more preferred buffer system uses gluconic acid and gluconate to set the pH.
  • the conversion alkali solutions preferably concentrated alkali solutions, can be added to neutralize the gluconic acid produced.
  • the amount of alkali consumed at constant pH provides an direct indication of the amount of gluconic acid produced.
  • the compound used to adjust the pH can be chosen accordingly, e.g. CaCO 3 will produce Ca- gluconate and NaOH will produce Na-gluconate.
  • protective agents are added to the enzymatic reaction in order to improve the performance of the enzymes involved.
  • the protective agents should improve the stability and/or protect the enzymes involved against oxidation.
  • protective agents include proteinaceous material, casein, methionine, quinine, or other compounds which can be oxidated by hydrogen peroxide.
  • the protective agents and/or the oxidated derivatives thereof are not toxic and/or can be easily removed from the final product, i.e. the gluconic acid solution.
  • the invention thus includes the addition of polyol compounds such as mannitol, sorbitol and glycerol.
  • the concentration of glucose in the syrup after the saccharification steps is between 30 and 40% w/w.
  • these syrups are further concentrated.
  • These solutions can be used directly for the conversion of glucose into gluconic acid in the process of the invention; the use of concentrated glucose solutions will result in the production of concentrated gluconic acid solution which do not, or to a lesser extend, require further energy-intensive concentration; the recovery, especially for the products which need a high purity, will be much more simple for the products obtained from the enzymatic process of the invention as compared to the products obtained from the fermentative process.
  • One International Catalase Unit (referred to as IU herein) is the enzyme activity which decomposes 1 /Mole H 2 O 2 per minute in 5 ml Phosphate buffer (0.01 M - pH 6.8) from an initial H 2 O 2 concentration of 2 mMoles.
  • the activity is then expressed in units per gram or ml of enzymatic solution.
  • the amount of decomposed H 2 O 2 is then calculated in reference to the initial absorbance of the substrate solution correctly diluted in the same volume mixture (containing 2 ml Sulphuric acid and 1 ml buffer instead of enzyme solution).
  • Glucose oxidase oxidizes glucose to gluconic acid and hydrogen peroxide. This latter is reduced to water by peroxidase in presence of a chromogen (hydrogen donor).
  • the optical density of the oxidized chromogen which becomes violet in acid medium, is a measure for the glucose oxidase activity.
  • One Sarett Unit is the quantity of enzyme causing in a Warburg manometer 10 mrrvVminute of oxygen consumption at 30°C by a 3.3% glucose solution in phosphate buffer pH 5.9 and with an excess of oxygen and catalase.
  • the substrate solution prepared in phtalate buffer 0.1 M pH 5.4 contains:
  • the activity measurement according to this colorimetric method is then expressed in Sarett units in reference to a calibration plot using glucose oxidase standard solutions at known Sarett units versus the corresponding colorimetric values.
  • the gluconic acid dosage was performed by using the D-gluconic acid test combination from Boehringer Mannheim (Cat. N ° 428-1 91 ).
  • D-gluconic acid is phosphorylated by ATP to gluconate 6-Phosphate.
  • gluconate 6-phosphate is oxidized by NADP to ribulose-5-phosphate with the formation of NADPH.
  • the amount of NADPH is stoichiometric with the amount of gluconic acid.
  • the increase in NADPH is determined by means of its absorbance at 340 nm.
  • the glucose concentration was assayed by using the Beckman Glucose Analyser 2.
  • Glucose is determined by means of the oxygen rate method employing oxygen electrode.
  • the glucose oxidase/catalase preparation referred to as 4056 herein was obtained by dissolving the commercially available Maxazym ® GO-P preparation, which is obtainable from Gist-brocades N.V., at the desired concentration.
  • the catalase-Gox ratio of this preparation is 1 .1 IU/SU.
  • the glucose oxidase preparations rich in catalase (referred to as L3052 and P3052 herein) were obtained by fermentation of the proprietary A.niger strain CBS 263.94.
  • the catalase-Gox ratios for these preparation are:
  • Enzyme preparations that are functionally identical to the "3052" preparations can be prepared by adding a commercially available A.niger catalase preparation, e.g. obtainable from Merck (see below), ICN (Cat. No. 1 9031 1 ) or from Genencor Int., to commercially obtainable glucose oxidase preparation such as the above described Maxazym ® GO-P preparation.
  • a commercially available A.niger catalase preparation e.g. obtainable from Merck (see below), ICN (Cat. No. 1 9031 1 ) or from Genencor Int.
  • Catalase from A. niger Merck
  • Catalase from Beef liver Boehringer; Cat. No. 1 06.828
  • the conversion of glucose into gluconic acid can be followed by :
  • the conversion starts immediately.
  • the dissolved oxygen concentration is almost zero.
  • the demand of sodium hydroxide starts immediately and is linear in the beginning. But already after about 30 minutes, the demand of sodium hydroxide and the oxygen consumption slow down, the dissolved oxygen concentration goes up and after 2 hours, the conversion has completely stopped. At that moment, less than 10% glucose is converted into gluconic acid.
  • Example 1 The experiment mentioned in Example 1 was repeated with the same results. When the conversion had stopped, a considerable amount of hydrogen peroxide was detected in the broth. At this point, we added 33 000 IU catalase/l without glucose oxidase activity (obtained from Merck). An immediate hydrolysis of the hydrogen peroxide could be seen by the formation of gas bubbles and the response of the dissolved oxygen concentration probe.
  • Table 1 summarizes the results obtained with the preparations and shows the influence of enzyme dosage and glucose concentration on the time required for complete conversion of glucose into gluconic acid.
  • Experiment 4,5 and 10 show that high glucose concentrations can be converted into gluconic acid. During the conversion, the dissolved oxygen concentration was almost zero. This means that it was not the amount of enzyme which was the rate limiting step but the oxygen transfer rate (OTR) .
  • OTR oxygen transfer rate
  • the OTR in experiment 10 is rather low due to high viscosity of the concentrated glucose solution which explains the relatively long conversion time.
  • the glucose solutions were buffered with a 0.05 M sodium phosphate buffer.
  • the use of buffers may result in extra costs, e.g. the phosphate salt may have a negative effect on the recovery of the gluconic acid or gluconate.
  • the conditions in the lab fermenter were: 360 g glucose/l, 25 °C, pH 6.0 (NaOH), air 1 VVM, glucose oxidase 5000 SU/I (enzyme preparation L3052).

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)

Abstract

Procédé enzymatique de conversion du glucose en acide gluconique à l'aide de solutions de glucose concentrées. Ledit procédé consiste à utiliser une combinaison d'enzymes glucose oxydase et catalase, qui peut être obtenue à partir d'une souche d'Aspergillus niger et qui possède un taux élevé d'activité catalase/glucose oxydase. Ledit procédé enzymatique exige moins de temps que les processus de fermentation traditionnels, le rendement de la conversion est proche de 100 % et les solutions d'acide gluconique/gluconate ainsi obtenues ne contiennent pas d'impuretés.
PCT/EP1996/002128 1995-05-12 1996-05-13 Production enzymatique d'acide gluconique ou de ses sels WO1996035800A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
JP53379896A JP3910213B2 (ja) 1995-05-12 1996-05-13 グルコン酸及びその塩の酵素的生産方法
CA002194859A CA2194859C (fr) 1995-05-12 1996-05-13 Production enzymatique d'acide gluconique ou de ses sels
AU59983/96A AU5998396A (en) 1995-05-12 1996-05-13 Enzymatic production of gluconic acid or its salts
US08/765,663 US5897995A (en) 1995-05-12 1996-05-13 Enzymatic production of gluconic acid or its salts

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP95201247 1995-05-12
EP95201247.4 1995-05-12

Publications (1)

Publication Number Publication Date
WO1996035800A1 true WO1996035800A1 (fr) 1996-11-14

Family

ID=8220291

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP1996/002128 WO1996035800A1 (fr) 1995-05-12 1996-05-13 Production enzymatique d'acide gluconique ou de ses sels

Country Status (8)

Country Link
US (1) US5897995A (fr)
JP (1) JP3910213B2 (fr)
AT (1) ATE216724T1 (fr)
AU (1) AU5998396A (fr)
CA (1) CA2194859C (fr)
DE (1) DE69620819T2 (fr)
NL (1) NL1003095C2 (fr)
WO (1) WO1996035800A1 (fr)

Cited By (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1997024454A1 (fr) * 1995-12-27 1997-07-10 Genencor International, Inc. Procede de preparation d'acide gluconique et acide gluconique ainsi produit
WO1998020136A1 (fr) * 1996-11-07 1998-05-14 Novo Nordisk Biotech, Inc. Glucose-oxydases
WO1999053088A1 (fr) * 1998-04-08 1999-10-21 Deva Processing Services Ltd. Preparation enzymatique de galactose et/ou d'acide gluconique a partir de di- ou polysaccharides
CN1054161C (zh) * 1997-12-17 2000-07-05 中山大学 黑曲霉发酵葡萄糖生产葡萄糖酸镁或葡萄糖酸锰
WO2003093489A1 (fr) * 2002-05-02 2003-11-13 Nec Partnership Production de sels de gluconate
US6828130B2 (en) 2000-05-23 2004-12-07 Nec Partnership Production of gluconate salts
EP1935257A1 (fr) * 2006-12-18 2008-06-25 Kraft Foods Holdings, Inc. Édulcorant acide et son procédé d'utilisation
EP2457990A1 (fr) 2010-11-29 2012-05-30 Sika Technology AG Procédé et dispositif pour la production d'acide gluconique
EP2532253A1 (fr) 2011-06-09 2012-12-12 RUDOLF WILD GmbH & CO. KG Procédé de préparation d'un aliment liquide concentré
EP2820961A1 (fr) 2013-07-03 2015-01-07 RUDOLF WILD GmbH & CO. KG Processus de fermentation enzymatique
CN107557396A (zh) * 2017-08-24 2018-01-09 南京林业大学 一种两阶段全细胞催化木质纤维水解液联产多种糖酸的方法

Families Citing this family (20)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20020119538A1 (en) * 1997-10-15 2002-08-29 Lantero Oreste J. Process for the preparation of gluconic acid and gluconic acid produced thereby
US6485761B1 (en) * 1999-02-24 2002-11-26 Novozymes Biotech, Inc. Methods for using lactonohydrolases in baking
CN1184472C (zh) 1999-10-05 2005-01-12 松下电器产业株式会社 葡萄糖传感器
FR2801901B1 (fr) 1999-12-07 2003-11-14 Roquette Freres Procede de transformation de matieres organiques, en particulier saccharidiques, comprenant une etape d'oxydation enzymatique en presence de ruthenium ou palladium
BR0114715A (pt) * 2000-10-21 2004-10-19 Bp Chemical Ltd Processo para a hidratação de olefinas
KR20030035140A (ko) * 2001-10-30 2003-05-09 주식회사 한바이오텍 글루콘산 제일철의 제조방법
CN1653031B (zh) 2002-03-13 2010-05-05 格雷斯公司 增效的减水组合物
KR20030096457A (ko) * 2002-06-12 2003-12-31 주식회사 한바이오텍 효소반응을 이용한 글루콘산 칼슘의 제조방법
NZ523100A (en) * 2002-12-10 2005-02-25 Fonterra Co Operative Group A process for producing a carbohydrate composition
CN100548913C (zh) * 2003-12-01 2009-10-14 格雷斯公司 含有粗葡萄糖发酵液的水泥组合物及其制备方法
CN101184702B (zh) * 2005-06-02 2017-08-08 Gcp应用技术有限公司 源自生物质的助磨剂
US8583204B2 (en) 2008-03-28 2013-11-12 Dexcom, Inc. Polymer membranes for continuous analyte sensors
US11730407B2 (en) 2008-03-28 2023-08-22 Dexcom, Inc. Polymer membranes for continuous analyte sensors
JP6732017B2 (ja) 2015-07-24 2020-07-29 アニッキ ゲーエムベーハーＡｎｎｉｋｋｉ Ｇｍｂｈ 糖混合物から酸化生成物および還元生成物を得るための方法
KR102523898B1 (ko) * 2018-02-20 2023-04-19 상-에이 도오까 가부시끼가이샤 당카르본산의 제조 방법
CN109280693A (zh) * 2018-11-12 2019-01-29 济南百斯杰生物工程有限公司 一种快速评价葡萄糖氧化酶产酸能力的方法
KR102114286B1 (ko) * 2020-03-17 2020-05-22 (주)더마랩 효소처리된 아가베시럽 추출물을 유효성분으로 함유하는 화장료 조성물
KR102635761B1 (ko) * 2021-06-14 2024-02-13 대상 주식회사 항산화 활성을 가지는 산화당류 조성물의 제조방법
CN116855550B (zh) * 2023-09-04 2023-11-17 山东福洋生物科技股份有限公司 一种酶法生产葡萄糖酸钠的方法
CN118147243B (zh) * 2024-03-26 2025-03-11 东晓生物科技股份有限公司 一种葡萄糖酸钠的制备方法

Citations (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR1590031A (fr) * 1968-10-28 1970-04-06
FR2029645A1 (fr) * 1969-01-29 1970-10-23 Cpc International Inc
FR2177931A1 (fr) * 1972-03-24 1973-11-09 Boehringer Mannheim Gmbh
FR2441658A1 (fr) * 1978-11-20 1980-06-13 Tno Enzyme immobilise, procedes pour la preparation dudit enzyme et procede pour la mise en oeuvre d'une reaction enzymatique
EP0017708A2 (fr) * 1979-03-22 1980-10-29 C.H. Boehringer Sohn Procédé pour l'oxydation enzymatique du glucose
GB2106521A (en) * 1981-09-21 1983-04-13 Novo Industri As Stabilised solutions of rennet
EP0114630A2 (fr) * 1983-01-21 1984-08-01 Winfried Prof. Dr. Ing. Hartmeier Mycélium de moisissures perméabilisé ayant un système glucose oxidase-catalase immobilisé intact, sa préparation et son application
RO92739A2 (fr) * 1985-10-01 1987-10-30 Intreprinderea De Medicamente"Terapia",Ro Procede d'obtention de l'acide gluconique
JPS6317690A (ja) * 1986-07-10 1988-01-25 Daiwa Kasei Kk 安定化された酵素水溶液
WO1991017235A1 (fr) * 1990-05-04 1991-11-14 Genencor International, Inc. Granules contenant a la fois une enzyme et un agent protecteur d'enzyme, et compositions de detergent contenant lesdits granules
US5292773A (en) * 1990-02-14 1994-03-08 Hirsch Gerald P Treating aids and HIV infection with methionine

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1249347A (en) * 1968-10-11 1971-10-13 Pabst Brewing Co Aldonic acid and aldonate compositions and production thereof
BE900723A (fr) * 1984-10-01 1985-02-01 Vangeenberghe Jacques Mecanisme d'articulation pour un lit-divan.
US6295836B1 (en) * 2000-04-14 2001-10-02 Praxair Technology, Inc. Cryogenic air separation system with integrated mass and heat transfer

Patent Citations (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR1590031A (fr) * 1968-10-28 1970-04-06
FR2029645A1 (fr) * 1969-01-29 1970-10-23 Cpc International Inc
FR2177931A1 (fr) * 1972-03-24 1973-11-09 Boehringer Mannheim Gmbh
FR2441658A1 (fr) * 1978-11-20 1980-06-13 Tno Enzyme immobilise, procedes pour la preparation dudit enzyme et procede pour la mise en oeuvre d'une reaction enzymatique
EP0017708A2 (fr) * 1979-03-22 1980-10-29 C.H. Boehringer Sohn Procédé pour l'oxydation enzymatique du glucose
GB2106521A (en) * 1981-09-21 1983-04-13 Novo Industri As Stabilised solutions of rennet
EP0114630A2 (fr) * 1983-01-21 1984-08-01 Winfried Prof. Dr. Ing. Hartmeier Mycélium de moisissures perméabilisé ayant un système glucose oxidase-catalase immobilisé intact, sa préparation et son application
RO92739A2 (fr) * 1985-10-01 1987-10-30 Intreprinderea De Medicamente"Terapia",Ro Procede d'obtention de l'acide gluconique
JPS6317690A (ja) * 1986-07-10 1988-01-25 Daiwa Kasei Kk 安定化された酵素水溶液
US5292773A (en) * 1990-02-14 1994-03-08 Hirsch Gerald P Treating aids and HIV infection with methionine
WO1991017235A1 (fr) * 1990-05-04 1991-11-14 Genencor International, Inc. Granules contenant a la fois une enzyme et un agent protecteur d'enzyme, et compositions de detergent contenant lesdits granules

Non-Patent Citations (7)

* Cited by examiner, † Cited by third party
Title
CHO ET AL.: "The influence of peroxide-stabilizing agents on enzyme deactivation by H2O2", BIOTECH. BIOENG., vol. 19, no. 1, 1977, pages 157 - 158, XP000578219 *
DATABASE WPI Week 8806, Derwent World Patents Index; AN 041008, XP002011045 *
DATABASE WPI Week 8809, Derwent World Patents Index; AN 88-061231, XP002011046 *
DÖPPNER ET AL.: "Glucose oxidation by modified mould mycelium", STARCH, vol. 36, no. 8, 1984, pages 283 - 287, XP002011043 *
HARTMEIER ET AL.: "Preparation and properties of mycelium bound glucose oxidase co-immobilized with excess catalase", BIOTECH. LETT., vol. 5, no. 11, 1983, pages 743 - 748, XP002011041 *
LIU ET AL.: "Enzymatic oxidation of glucose via crab chitin immobilized glucose oxidase and catalase", PROC. NATL SCI. COUNC. REPUB. CHINA, vol. 4, no. 3, 1980, pages 338 - 345, XP002011044 *
ROSENBERG ET AL.: "Gluconic acid production by Aspergillus niger with oxygen supply by hydrogen peroxide", BIOPROCESS. ENG., vol. 7, no. 7, 1992, pages 309 - 313, XP002011042 *

Cited By (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1997024454A1 (fr) * 1995-12-27 1997-07-10 Genencor International, Inc. Procede de preparation d'acide gluconique et acide gluconique ainsi produit
WO1998020136A1 (fr) * 1996-11-07 1998-05-14 Novo Nordisk Biotech, Inc. Glucose-oxydases
CN1054161C (zh) * 1997-12-17 2000-07-05 中山大学 黑曲霉发酵葡萄糖生产葡萄糖酸镁或葡萄糖酸锰
WO1999053088A1 (fr) * 1998-04-08 1999-10-21 Deva Processing Services Ltd. Preparation enzymatique de galactose et/ou d'acide gluconique a partir de di- ou polysaccharides
US6828130B2 (en) 2000-05-23 2004-12-07 Nec Partnership Production of gluconate salts
US7267970B2 (en) 2000-05-23 2007-09-11 Nec Partnership Production of gluconate salts
WO2003093489A1 (fr) * 2002-05-02 2003-11-13 Nec Partnership Production de sels de gluconate
EP1935257A1 (fr) * 2006-12-18 2008-06-25 Kraft Foods Holdings, Inc. Édulcorant acide et son procédé d'utilisation
EP2457990A1 (fr) 2010-11-29 2012-05-30 Sika Technology AG Procédé et dispositif pour la production d'acide gluconique
WO2012072591A1 (fr) 2010-11-29 2012-06-07 Sika Technology Ag Procédé et dispositif de production d'acide gluconique
EP2532253A1 (fr) 2011-06-09 2012-12-12 RUDOLF WILD GmbH & CO. KG Procédé de préparation d'un aliment liquide concentré
WO2012167872A1 (fr) 2011-06-09 2012-12-13 Rudolf Wild Gmbh & Co. Kg Procédé de préparation d'un produit alimentaire liquide concentré
EP2717724B1 (fr) * 2011-06-09 2016-04-06 Rudolf Wild GmbH & Co. KG Procédé de préparation d'un produit alimentaire liquide concentré
US10080380B2 (en) 2011-06-09 2018-09-25 ADM WILD Europe GmbH & Co. KG Process of preparing a concentrated liquid foodstuff
EP2820961A1 (fr) 2013-07-03 2015-01-07 RUDOLF WILD GmbH & CO. KG Processus de fermentation enzymatique
CN107557396A (zh) * 2017-08-24 2018-01-09 南京林业大学 一种两阶段全细胞催化木质纤维水解液联产多种糖酸的方法

Also Published As

Publication number Publication date
NL1003095A1 (nl) 1996-09-05
JP3910213B2 (ja) 2007-04-25
DE69620819D1 (de) 2002-05-29
AU5998396A (en) 1996-11-29
US5897995A (en) 1999-04-27
ATE216724T1 (de) 2002-05-15
CA2194859A1 (fr) 1996-11-14
DE69620819T2 (de) 2002-11-07
CA2194859C (fr) 2006-08-15
NL1003095C2 (nl) 1996-11-12
JPH10502825A (ja) 1998-03-17

Similar Documents

Publication Publication Date Title
US5897995A (en) Enzymatic production of gluconic acid or its salts
Anastassiadis et al. Gluconic acid production
EP1012323B1 (fr) Procede de production d'acides dicarboxyliques
US4221869A (en) Enzymatic synthesis of L-carnitine
Satory et al. Continuous enzymatic production of lactobionic acid using glucose-fructose oxidoreductase in an ultrafiltration membrane reactor
EP0705345B1 (fr) Procede de preparation de l'acide pyruvique
JPH02257885A (ja) グリセロールから１，３‐プロパンジオールを微生物学的に生成する方法
US4935360A (en) Process for the microbial anaerobic production of acetic acid
Nimcevic et al. Solvent production by Clostridium beijerinckii NRRL B592 growing on different potato media
EP0745677B1 (fr) Production enzymatique de l'acide gluconique et de ses sels
EP0244920A1 (fr) Procédé de préparation d'une oxydase exempte de catalase et d'une levure contenant une oxydase exempte de catalase et leur emploi
Cho et al. Glucoamylase and glucose oxidase preparations and their combined application for conversion of maltose to gluconic acid
Linek et al. Oxidation of D‐glucose in the presence of glucose oxidase and catalase
EP0242007B1 (fr) Procédé de préparation de levure contenant une oxidase exempte de catalase et son utilisation
US4473645A (en) Process for producing thermally stable alpha-amylase
Rosenberg et al. Gluconic acid production by Aspergillus niger with oxygen supply by hydrogen peroxide
US5234827A (en) Enzymatic process for manufacturing formaldehyde and hydrogen peroxide
US4734368A (en) Process for the bioconversion of fumarate to L-malate
JPS62253388A (ja) Ｌ−カルニチンの改良された製造方法
US5538875A (en) Process for the preparation of pyruvic acid using permeabilized transformants of H. polymorha and P. pastoris which express glycolate oxidase and catalase
US4169013A (en) Process for preparing glucoamylase
CA1209073A (fr) Procede biotechnique de production de l'acide l-malique
US3701715A (en) Method for the production of glucose oxidase
GB2218099A (en) Process for preparing a catalase-free oxidase
KR19990061564A (ko) 가압조건 하에서 포도당 산화효소를 이용한 글루콘산 칼슘의 제 조방법

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): AL AM AT AU AZ BB BG BR BY CA CH CN CZ DE DK EE ES FI GB GE HU IS JP KE KG KP KR KZ LK LR LS LT LU LV MD MG MK MN MW MX NO NZ PL PT RO RU SD SE SG SI SK TJ TM TR TT UA UG US UZ VN AM AZ BY KG KZ MD RU TJ TM

AL Designated countries for regional patents

Kind code of ref document: A1

Designated state(s): KE LS MW SD SZ UG BF BJ CF CG CI CM GA GN ML MR NE SN TD TG

WWE Wipo information: entry into national phase

Ref document number: 2194859

Country of ref document: CA

WWE Wipo information: entry into national phase

Ref document number: 08765663

Country of ref document: US

REG Reference to national code

Ref country code: DE

Ref legal event code: 8642

点击 这是indexloc提供的php浏览器服务，不要输入任何密码和下载